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2G3D

Structure of S65G Y66A GFP variant after spontaneous peptide hydrolysis

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL11-1
Synchrotron siteSSRL
BeamlineBL11-1
Temperature [K]100
Detector technologyCCD
Collection date2002-03-10
DetectorADSC QUANTUM 315
Wavelength(s)0.979
Spacegroup nameP 21 21 21
Unit cell lengths51.000, 62.600, 70.000
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 1.350
Rwork0.142
R-free0.21500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ema
RMSD bond length0.011
RMSD bond angle0.029
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.400
High resolution limit [Å]1.3501.350
Number of reflections49224
<I/σ(I)>25.33.6
Completeness [%]98.298.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP829850 mM MgCl2, 50 mM Hepes, 20% PEG 4000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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